Analytical Data
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Gene name
RBKS
- Application
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Alternative Names
RBKS; RBSK; Ribokinase; RK; EC 2.7.1.15
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H477
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Expression Region
2-322aa
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Molecular Weight
50 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
RBKS (Ribose-5-Phosphate Isomerase) is an essential enzyme involved in the pentose phosphate pathway, which plays a crucial role in cellular metabolism by generating ribose-5-phosphate, a precursor for nucleotide synthesis. Recent studies have highlighted the significance of RBKS not only in normal cellular functions but also in cancer metabolism, where altered metabolic pathways fuel rapid cell proliferation. The structural and functional characterization of RBKS has garnered interest due to its potential as a therapeutic target for cancer treatment. Researchers are focused on understanding the molecular mechanisms by which RBKS regulates metabolic fluxes and contributes to cellular redox balance. The reconstitution of RBKS as a recombinant protein allows for detailed biochemical studies, enabling the exploration of its enzymatic properties and interactions with other metabolic enzymes. This research paves the way for discovering small molecule inhibitors that could selectively target RBKS in cancer cells, thus opening new avenues for developing innovative cancer therapies aimed at disrupting aberrant metabolic pathways. The study of RBKS recombination and its implications for metabolic regulation is ongoing and presents an exciting frontier in metabolic research and cancer biology.
